MONOCLONAL-ANTIBODIES RECOGNIZE 2300 YEARS AGED ALKALINE-PHOSPHATASE

It was attempted to monitor the immunological response of monoclonal a ntibodies directed to human alkaline phosphatase in ancient Egyptian b ones from the ptolemeic period. The intactness of the respective epito pes of the bone enzyme was successfully demonstrated in an ELISA. Fort unately, the mummified bone was not contaminated by fungi and bacteria due to the fungicidal and bactericidal reactivity of the ancient pret reatment employing resins of pistachio for mummification. The enzyme w as enriched using gel chromatography, anion exchange and affinity chro matography to yield 310 +/- 7 mU/mg. The enzymically active fractions of the wheat-germ lectin affinity chromatography were subjected to ELI SA. The best binding affinity was detected using the monoclonal antibo dy BAP A while the reactions of all the other four antibodies BAP B, B AP G, BAP 4A5 and BAP 5D4 were substantially diminished.